(data stored in ACNUC7421 zone)

SWISSPROT: TAL_SYNFM

ID   TAL_SYNFM               Reviewed;         221 AA.
AC   A0LEA2;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 82.
DE   RecName: Full=Probable transaldolase {ECO:0000255|HAMAP-Rule:MF_00494};
DE            EC=2.2.1.2 {ECO:0000255|HAMAP-Rule:MF_00494};
GN   Name=tal {ECO:0000255|HAMAP-Rule:MF_00494};
GN   OrderedLocusNames=Sfum_0051;
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transaldolase is important for the balance of
CC       metabolites in the pentose-phosphate pathway. {ECO:0000255|HAMAP-
CC       Rule:MF_00494}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-
CC         phosphate = beta-D-fructose 6-phosphate + D-erythrose 4-
CC         phosphate; Xref=Rhea:RHEA:17053, ChEBI:CHEBI:16897,
CC         ChEBI:CHEBI:57483, ChEBI:CHEBI:57634, ChEBI:CHEBI:59776;
CC         EC=2.2.1.2; Evidence={ECO:0000255|HAMAP-Rule:MF_00494};
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-
CC       ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative
CC       stage): step 2/3. {ECO:0000255|HAMAP-Rule:MF_00494}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00494}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 3B
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_00494}.
DR   EMBL; CP000478; ABK15754.1; -; Genomic_DNA.
DR   RefSeq; WP_011696927.1; NC_008554.1.
DR   SMR; A0LEA2; -.
DR   STRING; 335543.Sfum_0051; -.
DR   EnsemblBacteria; ABK15754; ABK15754; Sfum_0051.
DR   KEGG; sfu:Sfum_0051; -.
DR   eggNOG; ENOG4105CW3; Bacteria.
DR   eggNOG; COG0176; LUCA.
DR   HOGENOM; HOG000226073; -.
DR   KO; K00616; -.
DR   OMA; VRHPMHV; -.
DR   OrthoDB; 784333at2; -.
DR   BioCyc; SFUM335543:G1G7I-53-MONOMER; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000001784; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
DR   GO; GO:0004801; F:sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniRule.
DR   CDD; cd00956; Transaldolase_FSA; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00494; Transaldolase_3b; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001585; TAL/FSA.
DR   InterPro; IPR022999; Transaldolase_3B.
DR   InterPro; IPR004731; Transaldolase_3B/F6P_aldolase.
DR   InterPro; IPR018225; Transaldolase_AS.
DR   InterPro; IPR033919; TSA/FSA_arc/bac.
DR   PANTHER; PTHR10683; PTHR10683; 1.
DR   Pfam; PF00923; TAL_FSA; 1.
DR   TIGRFAMs; TIGR00875; fsa_talC_mipB; 1.
DR   PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR   PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0LEA2.
DR   SWISS-2DPAGE; A0LEA2.
KW   Complete proteome; Cytoplasm; Pentose shunt; Reference proteome;
KW   Schiff base; Transferase.
FT   CHAIN         1    221       Probable transaldolase.
FT                                /FTId=PRO_1000126363.
FT   ACT_SITE     87     87       Schiff-base intermediate with substrate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00494}.
SQ   SEQUENCE   221 AA;  24224 MW;  EF123C85F5B0BC97 CRC64;
     MKFFIDTANL DEIKEAHSLG ILDGVTTNPS LIAKEGIANR EDFIRHIKTI CELIQAPVSA
     EAVSTDAEKM IVEARSLAAI DPHVVVKIPM TIDGLKAVRQ LSEEGIKTNV TLVFSPLQAL
     MAAKAGATYI SPFVGRLDDI SADGMNLVEE ILEIFSNYLF ETEIIVASVR NPLHVLAAAK
     LGADIATIPF KVIDQLAHHP LTDLGVERFL KDWEKVEKQR V
//

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